Biological diversity of cytochrome P450 redox partner systems

Kirsty J. McLean, Dominika Luciakova, James Belcher, Kang Lan Tee, Andrew W. Munro

Research output: Chapter in Book/Report/Conference proceedingChapter

28 Citations (Scopus)

Abstract

Cytochrome P450 enzymes (P450s or CYPs) catalyze an enormous variety of oxidative reactions in organisms from all major domains of life. Their monooxygenase activity relies on the reductive scission of molecular oxygen (O2) bound to P450 heme iron, and thus on the delivery of two electrons to the heme iron at discrete points in the catalytic cycle. Early studies suggested that P450 redox partner machinery fell into only two major classes: either the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase, or bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. However, more recent studies, aided by genome sequence data, reveal a much more complex scenario. Several new types of P450 redox partner systems have now been characterized, including P450s naturally linked to their redox partners, or to a component protein of their P450 electron delivery system. Other P450s have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis. Further P450s are fused to non-redox partner enzymes and can catalyse consecutive reactions in a common pathway. This chapter describes the biochemistry and the enormous natural diversity of P450 redox systems, including descriptions of novel P450s fused to non-redox partner proteins.

Original languageEnglish
Title of host publicationMonooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450
EditorsEugene G. Hrycay, Stelvio M. Bandiera
PublisherSpringer International Publishing
Chapter11
Pages299-317
Number of pages19
Volume851
Edition1st
ISBN (Electronic)9783319160092
ISBN (Print)9783319160085, 9783319347943
DOIs
Publication statusPublished - 30 Jun 2015
Externally publishedYes

Publication series

NameAdvances in Experimental Medicine and Biology
PublisherSpringer New York
Volume851
ISSN (Print)0065-2598
ISSN (Electronic)2214-8019

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  • Cite this

    McLean, K. J., Luciakova, D., Belcher, J., Tee, K. L., & Munro, A. W. (2015). Biological diversity of cytochrome P450 redox partner systems. In E. G. Hrycay, & S. M. Bandiera (Eds.), Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450 (1st ed., Vol. 851, pp. 299-317). (Advances in Experimental Medicine and Biology; Vol. 851). Springer International Publishing. https://doi.org/10.1007/978-3-319-16009-2_11